3e1p - Revision history

OCA at 12:56, 30 August 2023

2023-08-30T12:56:50Z

←Older revision		Revision as of 12:56, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='3e1p' size='340' side='right'caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3e1p' size='340' side='right'caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [https://pdbe.org/3e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [https://www.ebi.ac.uk/pdbsum/3e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1p ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [https://pdbe.org/3e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [https://www.ebi.ac.uk/pdbsum/3e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>	+	[https://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Brun, N Le]]~~	+	[[Category: Crow A]]
-	[[Category: Crow, A]]	+	[[Category: Lawson T]]
-	[[Category: Lawson, T]]	+	[[Category: Le Brun N]]
-	[[Category: ~~Lewin, A~~]]	+	[[Category: Lewin A]]
-	[[Category: ~~Moore, G R~~]]	+	[[Category: Moore GR]]
-	[[Category: ~~Bacterioferritin. rhombic dodecahedral superstructure]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Iron storage]]~~	+
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: Metal-binding~~]]	+

OCA at 08:13, 9 February 2022

2022-02-09T08:13:13Z

←Older revision		Revision as of 08:13, 9 February 2022
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	==Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.==		==Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.==
-	<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='3e1p' size='340' side='right'caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3E1P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [~~http~~://pdbe.org/3e1p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3e1p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1p ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [https://pdbe.org/3e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [https://www.ebi.ac.uk/pdbsum/3e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>	+	[[https://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Ferritin\|Ferritin]]	+	*[[Ferritin 3D structures\|Ferritin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Brun, N Le]]		[[Category: Brun, N Le]]
	[[Category: Crow, A]]		[[Category: Crow, A]]

OCA at 09:29, 14 November 2018

2018-11-14T09:29:23Z

←Older revision		Revision as of 09:29, 14 November 2018
Line 1:		Line 1:
		+
	==Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.==		==Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.==
	<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://pdbe.org/3e1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://pdbe.org/3e1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1p_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1p_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 02:21, 7 February 2016

2016-02-07T02:21:41Z

←Older revision		Revision as of 02:21, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://pdbe.org/3e1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e1p ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3e1p" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Brun, N Le]]		[[Category: Brun, N Le]]
	[[Category: Crow, A]]		[[Category: Crow, A]]

OCA at 07:03, 24 December 2014

2014-12-24T07:03:28Z

←Older revision		Revision as of 07:03, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1P FirstGlance]. <br>		<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1P FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Brun, N Le.]]	+	[[Category: Brun, N Le]]
-	[[Category: Crow, A.]]	+	[[Category: Crow, A]]
-	[[Category: Lawson, T.]]	+	[[Category: Lawson, T]]
-	[[Category: Lewin, A.]]	+	[[Category: Lewin, A]]
-	[[Category: Moore, G R.]]	+	[[Category: Moore, G R]]
	[[Category: Bacterioferritin. rhombic dodecahedral superstructure]]		[[Category: Bacterioferritin. rhombic dodecahedral superstructure]]
	[[Category: Heme]]		[[Category: Heme]]

OCA at 10:59, 29 September 2014

2014-09-29T10:59:49Z

←Older revision		Revision as of 10:59, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3e1p.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.==
		+	<StructureSection load='3e1p' size='340' side='right' caption='[[3e1p]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1P FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e1j\|3e1j]], [[3e1l\|3e1l]], [[3e1m\|3e1m]], [[3e1n\|3e1n]], [[3e1o\|3e1o]], [[3e1q\|3e1q]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e1p RCSB], [http://www.ebi.ac.uk/pdbsum/3e1p PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1p_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ferritin proteins function to detoxify, solubilize and store cellular iron by directing the synthesis of a ferric oxyhydroxide mineral solubilized within the protein's central cavity. Here, through the application of X-ray crystallographic and kinetic methods, we report significant new insight into the mechanism of mineralization in a bacterioferritin (BFR). The structures of nonheme iron-free and di-Fe(2+) forms of BFR showed that the intrasubunit catalytic center, known as the ferroxidase center, is preformed, ready to accept Fe(2+) ions with little or no reorganization. Oxidation of the di-Fe(2+) center resulted in a di-Fe(3+) center, with bridging electron density consistent with a mu-oxo or hydro bridged species. The mu-oxo bridged di-Fe(3+) center appears to be stable, and there is no evidence that Fe(3+)species are transferred into the core from the ferroxidase center. Most significantly, the data also revealed a novel Fe(2+) binding site on the inner surface of the protein, lying approximately 10 A directly below the ferroxidase center, coordinated by only two residues, His46 and Asp50. Kinetic studies of variants containing substitutions of these residues showed that the site is functionally important. In combination, the data support a model in which the ferroxidase center functions as a true catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins. The inner surface iron site appears to be important for the transfer of electrons, derived from Fe(2+) oxidation in the cavity, to the ferroxidase center. Bacterioferritin may represent an evolutionary link between ferritins and class II di-iron proteins not involved in iron metabolism.

-	~~{{STRUCTURE_3e1p\| PDB=3e1p \| SCENE= }}~~	+	Structural basis for iron mineralization by bacterioferritin.,Crow A, Lawson TL, Lewin A, Moore GR, Le Brun NE J Am Chem Soc. 2009 May 20;131(19):6808-13. PMID:19391621<ref>PMID:19391621</ref>

-	~~===Crystal structure~~ of ~~E. coli Bacterioferritin (BFR) in which~~ the ~~Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19391621}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3e1p]] is a 12 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA].~~	+

	==See Also==		==See Also==
	*[[Ferritin\|Ferritin]]		*[[Ferritin\|Ferritin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:019391621<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Brun, N Le.]]		[[Category: Brun, N Le.]]

OCA at 05:19, 20 October 2012

2012-10-20T05:19:47Z

←Older revision		Revision as of 05:19, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3e1p]] is a 12 chain structure ~~of [[Ferritin]]~~ with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA].	+	[[3e1p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA].

	==See Also==		==See Also==

OCA at 09:41, 25 July 2012

2012-07-25T09:41:37Z

←Older revision		Revision as of 09:41, 25 July 2012
Line 1:		Line 1:
	[[Image:3e1p.png\|left\|200px]]		[[Image:3e1p.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3e1p", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3e1p\| PDB=3e1p \| SCENE= }}		{{STRUCTURE_3e1p\| PDB=3e1p \| SCENE= }}

	===Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.===		===Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19391621}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19391621 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19391621}}		{{ABSTRACT_PUBMED_19391621}}

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	==See Also==		==See Also==
-	*[[Ferritin]]	+	*[[Ferritin\|Ferritin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19391621~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019391621</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Brun, N Le.]]		[[Category: Brun, N Le.]]

OCA: Protected "3e1p" [edit=sysop:move=sysop]

2010-12-26T08:35:35Z

Protected "3e1p" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:35, 26 December 2010

OCA at 08:35, 26 December 2010

2010-12-26T08:35:34Z

←Older revision		Revision as of 08:35, 26 December 2010
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3e1p.png\|left\|200px]]		[[Image:3e1p.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~3E1P~~ is a 12 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA].	+	[[3e1p]] is a 12 chain structure of [[Ferritin]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1P OCA].
		+
		+	==See Also==
		+	*[[Ferritin]]

	==Reference==		==Reference==
Line 36:		Line 38:
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 14:38:50 2009''